1d5y
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(New page: 200px<br /><applet load="1d5y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d5y, resolution 2.7Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 10:54, 20 November 2007
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CRYSTAL STRUCTURE OF THE E. COLI ROB TRANSCRIPTION FACTOR IN COMPLEX WITH DNA
Overview
The Escherichia coli Rob protein is a transcription factor belonging to, the AraC/XylS protein family that regulates genes involved in resistance, to antibiotics, organic solvents and heavy metals. The genes encoding, these proteins are activated by the homologous proteins MarA and SoxS, although the level of activation can vary for the different transcription, factors. Here we report a 2.7 A crystal structure of Rob in complex with, the micF promoter that reveals an unusual mode of binding to DNA. The, Rob-DNA complex differs from the previously reported structure of MarA, bound to the mar promoter, in that only one of Rob's dual helix-turn-helix, (HTH) motifs engages the major groove of the binding site. Biochemical, studies show that sequence specific interactions involving only one of, Rob's HTH motifs are sufficient for high affinity binding to DNA. The two, different modes of DNA binding seen in crystal structures of Rob and MarA, also match the distinctive patterns of DNA protection by AraC at several, sites within the pBAD promoter. These and other findings suggest that gene, activation by AraC/XylS transcription factors might involve two, alternative modes of binding to DNA in different promoter contexts.
About this Structure
1D5Y is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Escherichia coli Rob transcription factor in complex with DNA., Kwon HJ, Bennik MH, Demple B, Ellenberger T, Nat Struct Biol. 2000 May;7(5):424-30. PMID:10802742
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